Abstract: In order to explore the commonness and characteristics of wheat globulins in physicochemical properties and molecular structures,the physicochemical properties,multiple sequence alignments phylogenetic trees,conserved motifs,protein folding domain recognition and protein secondary structures of eight wheat globulins were analyzed by bioinformatics softwares including Protparam,Clustalw,MEME program3,and PSIPRED version 3.3 based on the existing NCBI protein database in present study. The results showed that the amino acid numbers of analyzed proteins ranged from 225 to 637 aa. The molecular weight distribution varied from 24.55 to 72.25 kDa. The theoretical isoelectric points were range of 5.22 to 8.72. The average hydrophilicities were the scope of -1.774 to 0.045. The coefficients of instability were varying from 36.02 to 77.64. The fat coefficients were the extent of 57.05 to 96.09. There were some conserved regions in multiple sequence alignments of wheat globulins,and six very conserved motifs in wheat globulins. The domain structure and folding domain structure of wheat globulins were less different. The secondary structures of wheat globulins(225~241 aa) were mainly composed of α-helices and random coils,and nearly nonexistent extended chains.However,the secondary structures of long wheat globulins (504~637 aa) were composed of α-helices,extended chains and random coils,as well as the ratio of the random coils,extended chains and α-helices was approximately 3:1:1. These results could provide biological data reference for the isolation,purification and utilization of wheat globulins.